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Reviewed, UniProtKB/Swiss-Prot Q5DZU8 (PANB2_VIBF1)

Last modified November 3, 2009. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-methyl-2-oxobutanoate hydroxymethyltransferase 2
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 2
      Short name=KPHMT 2
Gene names
Name: panB2
Ordered Locus Names: VF_A0628
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Complete proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate By similarity.

Catalytic activity

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP MF_00156

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP MF_00156

Subunit structure

Homodecamer; pentamer of dimers By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the panB family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpantothenate biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2632633-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156
PRO_0000297409

Regions

Region45 – 462Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding451Magnesium By similarity
Metal binding841Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site841Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5DZU8-1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 3BF5C3BBC17E463D

FASTA26328,601
        10         20         30         40         50         60 
MKKITISDLN NWKEVGEKFA SITAYDASFA KIFEEQSMPV IIVGDSLGSV IQGKPTTLDV 

        70         80         90        100        110        120 
SIEELVYHTK CVRAGSPNAF IISDLPFMSY HTPEAACGSA AKLMKAGANM VKIEGGSWLI 

       130        140        150        160        170        180 
NTVKMLTERA VPVCAHLGLM PQAVNIYGGY KLQGKTEEQA TKMLENAKEL QRAGAQALIL 

       190        200        210        220        230        240 
ECIPAKLARQ ITLELHIPVI GIGAGNDTDG QVLVMHDILG ISANYIPRFS RNFLAETGSI 

       250        260 
EAAVKKYIDE VKQQTFPGEK HCF 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed: 15703294] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000021 Genomic DNA. Translation: AAW87698.1. Different initiation.
RefSeqYP_206586.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5DZU8.

Genome annotation databases

GeneID3280238.
GenomeReviewsGene locus VF_A0628 in contig CP000021_GR.
KEGGvfi:VF_A0628.
NMPDRfig|312309.3.peg.3387.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5DZU8.
OMAMSYLLDP.

Enzyme and pathway databases

BioCycVFIS312309:VFA0628-MON.

Family and domain databases

HAMAPMF_00156.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
[Graphical view]
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
TIGRFAMsTIGR00222. panB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB2_VIBF1
AccessionPrimary (citable) accession number: Q5DZU8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: November 3, 2009
This is version 29 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents